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Conserved domains on  [gi|1622964299|ref|XP_028681852|]
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phosphotriesterase-related protein isoform X2 [Macaca mulatta]

Protein Classification

amidohydrolase family protein( domain architecture ID 330)

metal-dependent amidohydrolase family protein having a conserved metal binding site, usually involving four histidines and one aspartic acid residue

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
metallo-dependent_hydrolases super family cl00281
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
15-347 2.87e-140

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


The actual alignment was detected with superfamily member pfam02126:

Pssm-ID: 469705  Cd Length: 298  Bit Score: 399.63  E-value: 2.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAIAKEpimmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 175 PLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 255 LFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 1622964299 333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 2.87e-140

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 399.63  E-value: 2.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAIAKEpimmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 175 PLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 255 LFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 1622964299 333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 8.66e-133

Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active.


Pssm-ID: 238295  Cd Length: 293  Bit Score: 380.46  E-value: 8.66e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  21 GRTLTHEHLAMTFdccycppppcqEAIAKEPimmknlywiqknaysHKENLQLNQETEAIKEELLYFKANGGGALVENTT 100
Cdd:cd00530     1 GVTLTHEHLIIDS-----------SGFVRDP---------------PEVDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 101 TGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGVIGEIGCSWPLTESE 180
Cdd:cd00530    55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 181 KKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTIlDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530   135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 261 LHyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMK-YGGHGYSHILTNVVPKMLLRGITENVLDKILI 339
Cdd:cd00530   214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                  ....*..
gi 1622964299 340 ENPKQWL 346
Cdd:cd00530   287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 6.59e-101

Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction only];


Pssm-ID: 441341  Cd Length: 305  Bit Score: 299.78  E-value: 6.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299   5 SGKVQTVLGLVEPSKLGRTLTHEHLamTFDCCycppppcqeaiakepimmknlyWIQKNAYshKENLQLNQEtEAIKEEL 84
Cdd:COG1735     1 MGFVRTVLGPIPPEELGVTLMHEHL--FVDLP----------------------GVRQDPP--ADDDELDDV-EAAVEEL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  85 LYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKC 164
Cdd:COG1735    54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 165 GVIgEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISKTVMSHLDRTiLDKKELLE 243
Cdd:COG1735   134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 244 FAQLGCYLEYDLFGTELLHyqlcpdidmpDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735   211 LADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                         330       340
                  ....*....|....*....|....*
gi 1622964299 324 MLLRGITENVLDKILIENPKQWLTF 348
Cdd:COG1735   281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
78-345 1.05e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 131.49  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  78 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 157
Cdd:PRK09875   34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 158 DGTSIKCGVIGEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 235
Cdd:PRK09875  114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 236 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH 315
Cdd:PRK09875  193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622964299 316 ILTNVVPKMLLRGITENVLDKILIENPKQW 345
Cdd:PRK09875  261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
 
Name Accession Description Interval E-value
PTE pfam02126
Phosphotriesterase family;
15-347 2.87e-140

Phosphotriesterase family;


Pssm-ID: 396618  Cd Length: 298  Bit Score: 399.63  E-value: 2.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  15 VEPSKLGRTLTHEHLAMTFDCCYCPPPPCQEAIAKEpimmknlywiqknayshkenlqlnqeTEAIKEELLYFKANGGGA 94
Cdd:pfam02126   1 VEPSQLGRTLTHEHLTITFDSFYCNPPPCHEVTSKE--------------------------VAAIREELLYLKARGVGA 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  95 LVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGVIGEIGCSW 174
Cdd:pfam02126  55 LVENTTTGLGRDVHTLKWVAEQTGVNIVAGTGFYVDATHPAATRAMSVEQLTDVLVNEIEHGIDGTSIKAGIIGEIGCSW 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 175 PLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDrTILDKKELLEFAQLGCYLEYD 254
Cdd:pfam02126 135 PLTPSEEKVLEATAHAHAQTGCPISTHTGRNPGAGLQQIRILQEAGVDLSRVVMGHCD-TIFDKKELLEFIQLGCYLEYD 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 255 LFGTELlhyqlcpdidMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH--ILTNVVPKMLLRGITEN 332
Cdd:pfam02126 214 LFGYQL----------MPPDNKRIRRVHFLVDRGYEDRILLSHDIHTKHRLMKYGGHGYSHilIHTNIIPKLLQRGLTER 283
                         330
                  ....*....|....*
gi 1622964299 333 VLDKILIENPKQWLT 347
Cdd:pfam02126 284 VLDKMLIENPKQWFT 298
PTE cd00530
Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including ...
21-346 8.66e-133

Phosphotriesterase (PTE) catalyzes the hydrolysis of organophosphate nerve agents, including the chemical warfare agents VX, soman, and sarin as well as the insecticide paraoxon. PTE exists as a homodimer with one active site per monomer. The active site is located next to a binuclear metal center, at the C-terminal end of a TIM alpha- beta barrel motif. The native enzyme contains two zinc ions at the active site however these can be replaced with other metals such as cobalt, cadmium, nickel or manganese and the enzyme remains active.


Pssm-ID: 238295  Cd Length: 293  Bit Score: 380.46  E-value: 8.66e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  21 GRTLTHEHLAMTFdccycppppcqEAIAKEPimmknlywiqknaysHKENLQLNQETEAIKEELLYFKANGGGALVENTT 100
Cdd:cd00530     1 GVTLTHEHLIIDS-----------SGFVRDP---------------PEVDDFDLADVEAAKEELKRFRAHGGRTIVDATP 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 101 TGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKCGVIGEIGCSWPLTESE 180
Cdd:cd00530    55 PGIGRDVEKLAEVARATGVNIVAATGFYKDAFYPEWVRLRSVEELTDMLIREIEEGIEGTGIKAGIIKEAGGSPAITPLE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 181 KKVLQATAHAQAQLGCPVIIHPGRSSRAPFQIIRILQEAGADISKTVMSHLDRTIlDKKELLEFAQLGCYLEYDLFGTEL 260
Cdd:cd00530   135 EKVLRAAARAQKETGVPISTHTQAGLTMGLEQLRILEEEGVDPSKVVIGHLDRND-DPDYLLKIAALGAYLEFDGIGKDK 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 261 LHyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMK-YGGHGYSHILTNVVPKMLLRGITENVLDKILI 339
Cdd:cd00530   214 IF-------GYPSDETRADAVKALIDEGYGDRLLLSHDVFRKSYLEKrYGGHGYDYILTRFIPRLRERGVTEEQLDTILV 286

                  ....*..
gi 1622964299 340 ENPKQWL 346
Cdd:cd00530   287 ENPARFL 293
Php COG1735
Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction ...
5-348 6.59e-101

Predicted metal-dependent hydrolase, phosphotriesterase family [General function prediction only];


Pssm-ID: 441341  Cd Length: 305  Bit Score: 299.78  E-value: 6.59e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299   5 SGKVQTVLGLVEPSKLGRTLTHEHLamTFDCCycppppcqeaiakepimmknlyWIQKNAYshKENLQLNQEtEAIKEEL 84
Cdd:COG1735     1 MGFVRTVLGPIPPEELGVTLMHEHL--FVDLP----------------------GVRQDPP--ADDDELDDV-EAAVEEL 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  85 LYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGADGTSIKC 164
Cdd:COG1735    54 ERFKAAGGRTIVDATPIGLGRDPEALRRISEATGLNIVAATGFYKEPFHPEWVLGASVDELAELLIREITEGIDGTGVRA 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 165 GVIgEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPfQIIRILQEAGADISKTVMSHLDRTiLDKKELLE 243
Cdd:COG1735   134 GVI-KIGTSyGGITPDEEKVLRAAARAHRETGAPISTHTEAGTMGL-EQLDLLEEEGVDPERVVIGHMDRN-PDLDYHRE 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 244 FAQLGCYLEYDLFGTELLHyqlcpdidmpDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSHILTNVVPK 323
Cdd:COG1735   211 LADRGAYLEFDGIGRDKYY----------PDEERVELIAELIERGYADQILLSHDVGRKSYLKAYGGPGYDYILEVFLPR 280
                         330       340
                  ....*....|....*....|....*
gi 1622964299 324 MLLRGITENVLDKILIENPKQWLTF 348
Cdd:COG1735   281 LRRRGVTEEDIDTLLVDNPRRLFAF 305
PRK09875 PRK09875
phosphotriesterase-related protein;
78-345 1.05e-35

phosphotriesterase-related protein;


Pssm-ID: 182128  Cd Length: 292  Bit Score: 131.49  E-value: 1.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  78 EAIKEELLYFKANGGGALVENTTTGISRDTQTLKRLAEETGVHIISGAGFYVDATHSSETRAMSVEQLTDVLMNEILHGA 157
Cdd:PRK09875   34 AFICQEMNDLMTRGVRNVIEMTNRYMGRNAQFMLDVMRETGINVVACTGYYQDAFFPEHVATRSVQELAQEMVDEIEQGI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 158 DGTSIKCGVIGEIGCS-WPLTESEKKVLQATAHAQAQLGCPVIIHPGRSSRAPFQiIRILQEAGADISKTVMSHLD-RTI 235
Cdd:PRK09875  114 DGTELKAGIIAEIGSSeGKITPLEEKVFIAAALAHNQTGRPISTHTSFSTMGLEQ-LALLQAHGVDLSRVTVGHCDlKDN 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 236 LDKkeLLEFAQLGCYLEYDLFGTEllhyqlcpdiDMPDDNKRIRRVRLLVEEGYEDRILVAHDIHTKTRLMKYGGHGYSH 315
Cdd:PRK09875  193 LDN--ILKMIDLGAYVQFDTIGKN----------SYYPDEKRIAMLHALRDRGLLNRVMLSMDITRRSHLKANGGYGYDY 260
                         250       260       270
                  ....*....|....*....|....*....|
gi 1622964299 316 ILTNVVPKMLLRGITENVLDKILIENPKQW 345
Cdd:PRK09875  261 LLTTFIPQLRQSGFSQADVDVMLRENPSQF 290
TatD_DNase pfam01026
TatD related DNase; This family of proteins are related to a large superfamily of ...
67-346 1.46e-06

TatD related DNase; This family of proteins are related to a large superfamily of metalloenzymes. TatD, a member of this family has been shown experimentally to be a DNase enzyme.


Pssm-ID: 425997 [Multi-domain]  Cd Length: 253  Bit Score: 48.80  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299  67 HKENLQLNQETEAIKEEllyFKANGGGALVENTTTgiSRDTQTLKRLAEETGVHIISGAGFyvdatHSSEtramsVEQLT 146
Cdd:pfam01026   6 HLDFKDFDEDRDEVIER---AREAGVTGVVVVGTD--LEDFLRVLELAEKYPDRVYAAVGV-----HPHE-----ADEAS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 147 DVLMNEILHGADGTSIKCgvIGEIGC-SWPLTESEK----KVLQATAHAQAQLGCPVIIHpGRSSRApfQIIRILQEAGA 221
Cdd:pfam01026  71 EDDLEALEKLAEHPKVVA--IGEIGLdYYYVDESPKeaqeEVFRRQLELAKELGLPVVIH-TRDAEE--DLLEILKEAGA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622964299 222 DISKTVMSHLDrtiLDKKELLEFAQLGCYleydlFGtellhyqlCPDIDMPDDNKRIRRVRLLVEegyEDRILV---AHD 298
Cdd:pfam01026 146 PGARGVLHCFT---GSVEEARKFLDLGFY-----IS--------ISGIVTFKNAKKLREVAAAIP---LDRLLVetdAPY 206
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1622964299 299 IHTKTRLMKYGGHGYshiLTNVVPKML-LRGITENVLDKILIENPKQWL 346
Cdd:pfam01026 207 LAPVPYRGKRNEPAY---VPYVVEKLAeLKGISPEEVAEITTENAERLF 252
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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